Bone tissue response to an MTA-based endodontic sealer, and the effect of the addition of calcium aluminate and silver particles.

AIM: To evaluate bone tissue reactions in rats to an MTA-based endodontic sealer with and without the addition of various concentrations of C3A or C3A + Ag. METHODOLOGY: Bone tissue reactions were evaluated in 45 Wistar rats after 7, 30 and 90 days (n = 5 per period). Three surgical cavities were prepared on the right femur and filled with 0.2 mL MTA Fillapex, MTA Fillapex + C3A and C3A + Ag at various concentrations: AH Plus (Dentsply DeTrey GmbH, Konstanz, Germany), EndoSequence BC (Brasseler USA, Savannah, GA, USA) or no sealer (negative control). By the end of each experimental period, animals were randomly euthanized. The samples were histologically processed and analysed using a light microscope. The presence of inflammatory cells, fibres and hard tissue barrier formation was evaluated. Data were analysed statistically using nonparametric tests to compare the differences between groups. Multiple groups were compared using the Kruskal-Wallis and Mann-Whitney U-tests with a Bonferroni correction at P = 0.05. RESULTS: The inflammatory response significantly decreased from 30 to 90 days (P < 0.05). Fibre condensation was similar amongst the groups at 07 and 30 days after intervention (P > 0.05). At 90 days, however, fibres were absent in most specimens of EndoSequence BC Sealer, AH Plus, MTA Fillapex and the control group, whilst they were still observed in samples of the modified sealers (P < 0.05). At 90 days, all specimens of AH Plus, EndoSequence BC Sealer and control group had complete formation of hard tissue barrier. In the MTA Fillapex group, as well as in the modified sealers groups, partial deposition of mineralized tissue was noticed. CONCLUSION: The hypothesis tested that the incorporation of C3A and C3A + Ag particles to MTA Fillapex would improve bone tissue repair was partially accepted, since modified MTA Fillapex did not have the same repair potential as the commercial bioceramic material.

[Leptin: a parameter for metabolic changes in heart failure]. / Leptin: Ein Parameter für metabolische Veränderungen der Herzinsuffizienz.

OBJECTIVE: Advanced chronic heart failure is a hypercatabolic state with an imbalance between anabolic and catabolic metabolism and finally progressive loss of both muscle mass and adipose tissue. Leptin, the product of the obesity gene, is a hormone secreted by adipocytes. Therefore, we tested the hypothesis that plasma leptin concentrations are reduced in advanced chronic heart failure. METHODS: In 20 patients with chronic congestive heart failure (LVEF 23 +/- 6%) and 20 healthy controls (LVEF 65 +/- 8%) matched for gender, age, and body mass index, fasting plasma leptin (ELISA) and TNF alpha (ELISA) were measured. Follow-up examination was performed after 1 year. RESULTS: The fasting plasma leptin concentrations of patients with NYHA grade III (8.4 +/- 3.8 ng/ml*) and NYHA grade IV (4.6 +/- 2.4 ng/ml dagger) were significantly lower as compared with the controls (11.2 +/- 3.1 ng/ml; *p < 0.05, dagger p < 0.01). In patients with NYHA grade II plasma leptin levels were significantly elevated as compared with the healthy controls (14.9 +/- 4.2 ng/ml). TNF alpha was higher in heart failure patients than in healthy controls (8.6 +/- 3.6 pg/ml; 5.9 +/- 2.1 pg/ml; respectively; p < 0.05), but did not correlate with the NYHA functional class. Mortality of the controls was 0%, whereas 15% (n = 3) in the congestive heart failure group; one patient (5%) needs an urgent heart transplantation. All of those patients had leptin concentrations below 5 ng/ml. CONCLUSIONS: Plasma leptin concentrations correlate with the NYHA functional class suggesting anabolic metabolism in NYHA class II and catabolic metabolism in advanced heart failure which might be of prognostic relevance.

Structural organization of the porcine and human genes coding for a Leydig cell-specific insulin-like peptide (LEY I-L) and chromosomal localization of the human gene (INSL3).

Leydig insulin-like protein (LEY I-L) is a member of the insulin-like hormone superfamily. The LEY I-L gene (designated INSL3) is expressed exclusively in prenatal and postnatal Leydig cells. We report here the cloning and nucleotide sequence of porcine and human LEY I-L genes including the 5' regions. Both genes consist of two exons and one intron. The organization of the LEY I-L gene is similar to that of insulin and relaxin. The transcription start site in the porcine and human LEY I-L gene is localized 13 and 14 bp upstream of the translation start site, respectively. Alignment of the 5' flanking regions of both genes reveals that the first 107 nucleotides upstream of the transcription start site exhibit an overall sequence similarity of 80%. This conserved region contains a consensus TATAA box, a CAAT-like element (GAAT), and a consensus SP1 sequence (GGGCGG) at equivalent positions in both genes and therefore may play a role in regulation of expression of the LEY I-L gene. The porcine and human genome contains a single copy of the LEY I-L gene. By in situ hybridization, the human gene was assigned to bands p13.2-p12 of the short arm of chromosome 19.